Evaluation of new base-labile 2-(4-nitrophenylsulfonyl) ethoxycarbonyl (Nsc)-amino acids for solid-phase peptide synthesis

Journal of Peptide Research

Volumn 56, Issue 2, 2000, Pages 70-79

  Balse, P M ^a   Kim, H J ^b   Han, G ^a   Hruby, Victor J ^a  

^a University of Arizona   (United States)

^b Hyundai Pharm Ind Co Ltd   (South Korea)

Author keywords

2 (4 nitrophenylsulfonyl)ethoxycarbonyl; Base labile; Fmoc; Melanotropin; MSH; Nsc; Peptide; Protecting group; Solid phase; Synthesis

Indexed keywords

ALPHA INTERMEDIN; AMINO ACID DERIVATIVE; BETA INTERMEDIN; CARBONYL DERIVATIVE; GAMMA INTERMEDIN;

AMINO ACID SEQUENCE; ANALYTIC METHOD; ARTICLE; CHEMICAL BINDING; PEPTIDE SYNTHESIS; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN STRUCTURE;

AMINO ACID SEQUENCE; AMINO ACIDS; DISULFIDES; EVALUATION STUDIES; FLUORENES; MELANOCYTE-STIMULATING HORMONES; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDE BIOSYNTHESIS;

EID: 0033865465     PISSN: 1397002X     EISSN: None     Source Type: Journal    
DOI: 10.1034/j.1399-3011.2000.00759.x     Document Type: Article

References (25)

1. 1. Fields, G.B. & Noble, R.L. (1990) Solid-phase peptide-synthesis utilizing 9-fluorenylmethoxycarbonyl amino-acids. Int. J. Peptide Protein Res. 35, 161-214.
2. 2. Atherton, E., Bury, C. & Sheppard, R.C. (1979) Stability of fluorenylmethoxy-carbonylamino groups in peptide-synthesis: cleavage by hydrogenolysis and by dipolar aprotic solvents. Tetrahedron Lett. 32, 3041-3042.
3. 3. Fontenot, J.D., Ball, J.M., Miller, M.A., David, C.M. & Montelaro, R.C. (1991) A survey of potential problems and quality control in peptide synthesis by the fluorenylmethoxycarbonyl procedure. Peptide Res. 4, 19-25.
4. 4. Bodanszky, M., Deshmane, S.S. & Martinez, J. (1979) Side reactions in peptide-synthesis. II. Possible removal of the 9-fluorenylmethyloxycarbonyl group by the amino components during coupling. J. Org. Chem. 44, 1622-1625.
5. 5. Carpino, L.A. (1987) The 9-fluorenylmethyloxycarbonyl family of base-sensitive amino-protecting groups. Accounts Chem. Res. 20, 401-407.
6. 6. Sabirov, A.N., Kim, Y.D., Kim, H.J. & Samukov, V.V. (1997) FMOC-and NSC-groups as a base-labile N(alpha)-amino protection: a comparative study in the automated SPPS. Protein Peptide Lett. 4, 301-307.
7. 7. Hadley, M.E., Hruby, V.J., Blanchard, J., Dorr, R.T., Levine, N., Dawson, B.V., Al-Obeidi, F. & Sawyer, T.K. (1998) Discovery and development of novel melanogenic drugs: melanotan I and II. In Integration of Pharmaceutical Discovery and Development: Case Studies (Borchardt, R., ed.). Plenum Press, New York, pp. 575-596.
8. 8. Castrucci, A.M.L., Hadley, M.E., Sawyer, T.K., Wilkes, B.C., Al-Obeidi, F., Staples, D.J., Devaux, A.E., Dym, O., Hintz, M.F., Reihm, J.P., Rao, K.R. & Hruby, V.J. (1989) Alpha-melanotropin: the minimal active sequence in the lizard skin bioassay. Gen. Comp. Endocrinol. 73, 157-163.
9. 9. Hruby, V.J., Wilkes, B.C., Hadley, M.E., Al-Obeidi, F., Sawyer, T.K., Staples, D.J., Devaux, A.E., Dym, O., Castrucci, A.M.D., Hintz, M.F., Reihm, J.P. & Rao, K.R. (1987) Alpha-melanotropin: the minimal active sequence in the frog-skin bioassay. J. Med. Chem. 30, 2126-2130.
10. 10. Kaiser, E., Colescott, R.L., Bossinger, C.D. & Cook, P.I. (1970) Color test for detection of free terminal amino groups in the solid-phase synthesis of peptides. Anal. Biochem. 34, 595-598.
11. 11. Stewart, J.M. & Young, J.D. (1984) Laboratory techniques in solid phase synthesis. In Solid Phase Peptide Synthesis. Pierce Chemical Company, Rockford, IL, pp. 53-124.
12. 12. Wang, S.S. (1973) Para-alkoxybenzyl alcohol resin and para-alkoxybenzyloxy-carbonylhydrazide resin for solid-phase synthesis of protected peptide fragments. J. Am. Chem. Soc. 95, 1328-1333.
13. 13. Rink, H. (1987) Solid-phase synthesis of protected peptide-fragments using a trialkoxy-diphenylmethylester resin. Tetrahedron Lett. 28, 3787-3790.
14. 14. Pearson, D.A. (1989) Trialkylsilanes as scavengers for the trifluoroacetic acid deblocking of protecting groups in peptide-synthesis. Tetrahedron Lett. 30, 2739-2742.
15. 15. White, P. (1992) Fmoc-Trp(Boc)-OH: a new derivative for the synthesis of peptides containing tryptophan. In Peptides: Chemistry and Biology, Proceedings of the 12th American Peptide Symposium (Smith, J.A. & Rivier, J.E., eds). ESCOM, Leiden, pp. 537-538.
16. 16. Fields, C.G. & Fields, G.B. (1993) Minimization of tryptophan alkylation following 9-fluorenylmethoxycarbonyl solid-phase peptide-synthesis. Tetrahedron Lett. 34, 6661-6664.
17. 17. McCurdy, S.N. (1989) The investigation of Fmoc-cysteine derivatives in solid phase peptide synthesis. Peptide Res. 2, 147-152.
18. 18. Pohl, M., Ambrosius, D., Grotzinger, J., Kretzschmar, T., Saunders, D., Wollmer, A., Branderburg, D., Bittersuermann, D. & Hocker, H. (1993) Cyclic disulfide analogs of the complement component C3A: synthesis and conformational investigations. Int. J. Peptide Protein Res. 41, 362-375.
19. 19. Otaka, A., Koide, T., Shide, A. & Fujii, N. (1991) Application of dimethyl-sulphoxide (DMSO)/trifluoroacetic acid (TFA) oxidation to the synthesis of cystine-containing peptide. Tetrahedron Lett. 32, 1223-1226.
20. 20. Tam, J.P., Wu, C.R., Liu, W. & Zhang, J.W. (1991) Disulfide bond formation in peptides by dimethylsulfoxide: scope and applications. J. Am. Chem. Soc 113, 6657-6662.
21. 21. Ferrer, M., Woodward, C. & Barany, G. (1992) Solid-phase synthesis of bovine pancreatic trypsin inhibitor (BPTI) and two analogs: a chemical approach for evaluating the role of disulfide bridges in protein folding and stability. Int. J. Peptide Protein Res. 40, 194-207.
22. 22. Misicka, A. & Hruby, V.J. (1994) Optimization of disulfide bond formation. Polish J. Chem. 68, 893-899.
23. 23. Yajima, H., Fujii, N., Funakoshi, S., Watanabe, T., Murayama, E. & Otaka, A. (1988) New strategy for the chemical synthesis of proteins. Tetrahedron 44, 805-819.
24. 24. Nicolas, E., Vilaseca, M. & Giralt, E. (1994) Reduction of methionine sulfoxide in disulfide containing peptides. In Innovations and Perspectives in Solid-Phase Synthesis, Collected Papers of the 3rd International Symposium (Epton, R., ed.). Mayflower Worldwide Ltd., Birmingham, UK, pp. 619-622.
25. 1H distances in proteins. In NMR of Proteins and Nucleic Acids (Wüthrich, K., ed.). John Wiley & Sons, New York, pp. 117-129.